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  A Molecular Dynamics Model for Glycosylphosphatidyl-Inositol Anchors: "flop down" or "lollipop"?

Banerjee, P., Wehle, M., Lipowsky, R., & Santer, M. (2018). A Molecular Dynamics Model for Glycosylphosphatidyl-Inositol Anchors: "flop down" or "lollipop"? Physical Chemistry Chemical Physics, 20(46), 29314-29324. doi:10.1039/C8CP04059A.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-7AA5-B Version Permalink: http://hdl.handle.net/21.11116/0000-0002-BC55-B
Genre: Journal Article

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 Creators:
Banerjee, Pallavi1, Author              
Wehle, Marko2, Author              
Lipowsky, Reinhard3, Author              
Santer, Mark2, Author              
Affiliations:
1Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863289              
2Mark Santer, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863326              
3Reinhard Lipowsky, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863327              

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 Abstract: We present a computational model of glycosylphosphatidyl-inositol (GPI) anchors for molecular dynamics studies. The model is based on state-of-the-art biomolecular force fields from the AMBER family, employing GLYCAM06 for carbohydrates and Lipid14 to represent fatty acid tails. We construct an adapted glycero-phosphatidyl-inositol unit to establish a seamless transition between the two domains of atom types. This link can readily be extended into a broad variety of GPI variants by applying either domain's building block scheme. As test cases, selected GPI fragments inserted into DMPC and POPC bilayer patches are considered. Our results suggest that the glycan part of the GPI anchor interacts strongly with the lipid head groups, partially embedding the carbohydrate moieties. This behaviour is supported by the conformational preferences of the GPI anchor, which in particular are conveyed by the strong interactions between the proximal amine and phosphate groups. In a similar way we can conclude that the extension of the anchor away from the lipid bilayer surface that could prevent the contact of the membrane with an attached protein ("lollipop" picture") is quite unfavorable. Indeed, when attaching green fluorescent protein to the GPI anchor, it is found to reside close to bilayer surface all the time, and the rather flexible phosphoethanolamine linker governs the extent to which the protein directly interacts not only with the head groups, but also with its own GPI core.

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Language(s): eng - English
 Dates: 2018-11-092018
 Publication Status: Published in print
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 Identifiers: DOI: 10.1039/C8CP04059A
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Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
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Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: - Volume / Issue: 20 (46) Sequence Number: - Start / End Page: 29314 - 29324 Identifier: ISSN: 1463-9076